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Q7LZG2

- PA2T_OXYSC

UniProt

Q7LZG2 - PA2T_OXYSC

Protein

Phospholipase A2 taicatoxin

Gene
N/A
Organism
Oxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Heterotrimer: blocks the voltage-dependent L-type calcium channels from the heart, and the small conductance calcium-activated potassium channels in the chromaffin cells and in the brain. Is very toxic to mice.
    Monomer: Snake venom phospholipase A2 (PLA2) that has neurotoxic activities. Voltage-dependently affects ionic currents in chick (Gallus domesticus) dorsal root ganglion cells. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.

    Catalytic activityi

    Phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate.PROSITE-ProRule annotation

    Cofactori

    Binds 1 calcium ion.By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phospholipase A2 activity Source: UniProtKB-EC

    GO - Biological processi

    1. lipid catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Ion channel impairing toxin, Neurotoxin, Potassium channel impairing toxin, Toxin

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phospholipase A2 taicatoxin (EC:3.1.1.4)
    Short name:
    TCX
    Short name:
    svPLA2
    Alternative name(s):
    Phosphatidylcholine 2-acylhydrolase
    OrganismiOxyuranus scutellatus scutellatus (Australian taipan) (Coastal taipan)
    Taxonomic identifieri8667 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeAcanthophiinaeOxyuranus

    Subcellular locationi

    Secreted 2 Publications

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Toxic dosei

    LD50 of the monomer is 500 µg/kg to mice.
    LD50 of the heterotrimer is 50-100 µg/kg to mice.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›27›27Phospholipase A2 taicatoxinPRO_0000408515Add
    BLAST

    Post-translational modificationi

    Contains 7 disulfide bonds.By similarity

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.2 Publications

    Interactioni

    Subunit structurei

    Heterotrimer composed of an alpha-neurotoxin-like peptide of 8 kDa (AC P0CJ35), this neurotoxic phospholipase of 16 kDa and a serine protease inhibitor of 7 kDa (AC B7S4N9) at an approximate stoichiometry of 1:1:4; non-covalently linked.1 Publication

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR016090. PLipase_A2_dom.
    [Graphical view]
    PfamiPF00068. Phospholip_A2_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF48619. SSF48619. 1 hit.

    Sequencei

    Sequence statusi: Fragment.

    Q7LZG2-1 [UniParc]FASTAAdd to Basket

    « Hide

    NLAQFGFMIR CANGGSRSAL DYADYGC                            27
    Length:27
    Mass (Da):2,901
    Last modified:December 15, 2003 - v1
    Checksum:iA74F18ACB843133C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-terminal residuei27 – 271

    Sequence databases

    PIRiA34280.
    S21101.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Taicatoxin entry

    Sequence databases

    PIRi A34280.
    S21101.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR016090. PLipase_A2_dom.
    [Graphical view ]
    Pfami PF00068. Phospholip_A2_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48619. SSF48619. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Anionic currents of chick sensory neurons are affected by a phospholipase A2 purified from the venom of the taipan snake."
      Possani L.D., Mochca-Morales J., Amezcua J., Martin B.M., Prestipino G., Nobile M.
      Biochim. Biophys. Acta 1134:210-216(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, LETHAL DOSE.
      Tissue: Venom.
    2. "Isolation and physiological characterization of taicatoxin, a complex toxin with specific effects on calcium channels."
      Possani L.D., Martin B.M., Yatani A., Mochca-Morales J., Zamudio F.Z., Gurrola G.B., Brown A.M.
      Toxicon 30:1343-1364(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, LETHAL DOSE.
      Tissue: Venom.
    3. "Effect of TaiCatoxin (TCX) on the electrophysiological, mechanical and biochemical characteristics of spontaneously beating ventricular cardiomyocytes."
      Fantini E., Athias P., Tirosh R., Pinson A.
      Mol. Cell. Biochem. 160:61-66(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "A novel small conductance Ca2+-activated K+ channel blocker from Oxyuranus scutellatus taipan venom. Re-evaluation of taicatoxin as a selective Ca2+ channel probe."
      Doorty K.B., Bevan S., Wadsworth J.D.F., Strong P.N.
      J. Biol. Chem. 272:19925-19930(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Taicatoxin inhibits the calcium-dependent slow motility of mammalian outer hair cells."
      Su M.-C., Lee S.-Y., Tan C.-T., Su C.-C., Li S.-Y., Lin R.-H., Hung C.-C., Lin M.-J.
      Hear. Res. 203:172-179(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiPA2T_OXYSC
    AccessioniPrimary (citable) accession number: Q7LZG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 31, 2011
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 50 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3